Open AccessPeriplasmic Binding Protein Dimer Has a Second Allosteric Event Tied to Ligand Binding
Author(s) -
Le Li,
Sudipa Ghimire-Rijal,
Sarah L. Lucas,
Christopher B. Stanley,
Edward Wright,
Pratul K. Agarwal,
Dean A. A. Myles,
M.J. Cuneo
Publication year - 2017
Publication title -
biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.43
H-Index - 253
eISSN - 1520-4995
pISSN - 0006-2960
DOI - 10.1021/acs.biochem.7b00657
Subject(s) - periplasmic space , allosteric regulation , atp hydrolysis , ligand (biochemistry) , conformational change , chemistry , atp binding cassette transporter , biophysics , dimer , plasma protein binding , transporter , protein structure , biochemistry , binding site , biology , enzyme , atpase , receptor , organic chemistry , escherichia coli , gene
The ligand-induced conformational changes of periplasmic binding proteins (PBP) play a key role in the acquisition of metabolites in ATP binding cassette (ABC) transport systems. This conformational change allows for differential recognition of the ligand occupancy of the PBP by the ABC transporter. This minimizes futile ATP hydrolysis in the transporter, a phenomenon in which ATP hydrolysis is not coupled to metabolite transport. In many systems, the PBP conformational change is insufficient at eliminating futile ATP hydrolysis. Here we identify an additional state of the PBP that is also allosterically regulated by the ligand. Ligand binding to the homodimeric apo PBP leads to a tightening of the interface α-helices so that the hydrogen bonding pattern shifts to that of a 3 10 helix, in-turn altering the contacts and the dynamics of the protein interface so that the monomer exists in the presence of ligand.
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